Cited by 653Glycosylation and Glycoproteins ResearchGalectins and Cancer BiologyT-cell and B-cell Immunology

Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death

Toscano, Marta A, Bianco, Germán A, Ilarregui, Juan M, Croci, Diego O, Correale, Jorge, Hernandez, Joseph D, Zwirner, Norberto W, Poirier, Francoise +3 more·2007·Nature Immunology

Abstract

Regulated glycosylation controls T cell processes, including activation, differentiation and homing by creating or masking ligands for endogenous lectins. Here we show that stimuli promoting T helper type 1 (TH1), TH2 or interleukin 17-producing T helper (TH-17) differentiation can differentially regulate the glycosylation pattern of T helper cells and modulate their susceptibility to galectin-1, a glycan-binding protein with anti-inflammatory activity. Although TH1- and TH-17-differentiated cells expressed the repertoire of cell surface glycans critical for galectin-1-induced cell death, TH2 cells were protected from galectin-1 through differential sialylation of cell surface glycoproteins. Consistent with those findings, galectin-1-deficient mice developed greater TH1 and TH-17 responses and enhanced susceptibility to autoimmune neuroinflammation. Our findings identify a molecular link among differential glycosylation of T helper cells, susceptibility to cell death and termination of the inflammatory response.

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Crossref · 10.1038/ni1482

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  • Glycosylation state of some death receptors (e.g., FAS) impacts sensitivity of T lymphocytes to extrinsic apoptosis, influencing termination of inflammatory responses.

    “Of note, the glycosylation state of some death receptors (e.g., FAS) has been shown to impact on the sensitivity of T lymphocytes to extrinsic apoptosis, hence influencing the termination of inflammatory responses [288–290].”

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Authors
Toscano, M. A., Bianco, G. A., Ilarregui, J. M., Croci, D. O., Correale, J., Hernandez, J. D., Zwirner, N. W., Poirier, F., Riley, E. M., Baum, L. G., & Rabinovich, G. A.
Affiliations
  • Universidad de Buenos Aires (AR)
  • Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
  • University of California, Los Angeles (US)
  • London School of Hygiene & Tropical Medicine (GB)
Corresponding author
Rabinovich, Gabriel A
Venue
Nature Immunology
Published
2007-06-24
Volume
8
Issue
8
Pages
825-834
ISSN
  • 1529-2908 (ISSN-L)
  • 1529-2916
OpenAlex
W2041659209
Cited by
653
References
52
Citations by year
2026: 22 · 2025: 28 · 2024: 22 · 2023: 22 · 2022: 46 · 2021: 31 · 2020: 35 · 2019: 20 · 2018: 36 · 2017: 25 · 2016: 33 · 2015: 36 · 2014: 37 · 2013: 34 · 2012: 40
FWCI
18.17
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Immunology (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
Funders
Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Keywords
galectin-1, T helper cell differentiation, Th1 cells, Th2 cells, Th17 cells, sialylation, cell death, cell surface glycans, lectin binding, autoimmune neuroinflammation
MeSH terms
Animals, Cell Differentiation, Encephalomyelitis, Autoimmune, Experimental, Flow Cytometry, Glycosylation, T-Lymphocytes, Helper-Inducer, Humans, Inflammation, Membrane Glycoproteins, Polysaccharides, Immunoblotting, T-Lymphocyte Subsets, Apoptosis, Th1 Cells, Th2 Cells, Adoptive Transfer, In Situ Nick-End Labeling, Interleukin-17, Galectin 1, Mice

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